Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T79724 Target Info
Target Name Bacterial Hydroxymethyl-dihydropterin pyrophosphokinase (Bact folK)
Synonyms PPPK; HPPK; 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
Target Type Literature-reported Target
Gene Name Bact folK
Biochemical Class Kinase
UniProt ID
HPPK_ECOLI
Ligand General Information  Top
Ligand Name 6-Hydroxymethylpterin Ligand Info
Canonical SMILES C1=C(N=C2C(=O)NC(=NC2=N1)N)CO
InChI 1S/C7H7N5O2/c8-7-11-5-4(6(14)12-7)10-3(2-13)1-9-5/h1,13H,2H2,(H3,8,9,11,12,14)
InChIKey XGWIBNWDLMIPNF-UHFFFAOYSA-N
PubChem Compound ID 135415975
Drug Binding Sites of Target  Top
PDB ID: 3IP0      Crystal structure of E. coli HPPK in complex with MgAMPCPP and 6-hydroxymethylpterin/6-carboxypterin
Method X-ray diffraction Resolution 0.89 Å Mutation No [1]
PDB Sequence
TVAYIAIGSN
10
LASPLEQVNA
20
ALKALGDIPE
30
SHILTVSSFY
40
RTPPLGPQDQ
50

PDYLNAAVAL
60
ETSLAPEELL
70
NHTQRIELQQ
80
GRVRKAERWG
90
PRTLDLDIML
100

FGNEVINTER
110
LTVPHYDMKN
120
RGFMLWPLFE
130
IAPELVFPDG
140
EMLRQILHTR
150

AFDKLNKW
Residue
Distance (Å)
GLY8
3.452
THR42
2.531
PRO43
2.338
PRO44
2.902
LEU45
2.214
GLY46
3.896
ASP52
4.821
TYR53
2.764
Residue
Distance (Å)
ASN55
1.854
TRP89
2.246
ARG92
2.041
ASP95
2.600
ASP97
4.033
TYR116
4.758
ARG121
2.756
PHE123
2.812
PDB ID: 1TMM      Crystal structure of ternary complex of E.coli HPPK(W89A) with MGAMPCPP and 6-Hydroxymethylpterin
Method X-ray diffraction Resolution 1.25 Å Mutation Yes [2]
PDB Sequence
TVAYIAIGSN
10
LASPLEQVNA
20
ALKALGDIPE
30
SHILTVSSFY
40
RTPPLGPQDQ
50

PDYLNAAVAL
60
ETSLAPEELL
70
NHTQRIELQQ
80
GRVRKAERAG
90
PRTLDLDIML
100

FGNEVINTER
110
LTVPHYDMKN
120
RGFMLWPLFE
130
IAPELVFPDG
140
EMLRQILHTR
150

AFDKLNKW
Residue
Distance (Å)
GLY8
4.467
THR42
2.804
PRO43
2.802
PRO44
3.674
LEU45
3.114
TYR53
3.303
ASN55
2.810
Residue
Distance (Å)
ALA89
4.984
ARG92
3.850
ASP95
2.868
ASP97
4.144
ARG121
4.606
PHE123
3.227
PDB ID: 1RU2      CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E.COLI HPPK(V83G/DEL84-89) WITH MGAMPCPP AND 6-HYDROXYMETHYLPTERIN AT 1.48 ANGSTROM RESOLUTION (ORTHORHOMBIC FORM)
Method X-ray diffraction Resolution 1.48 Å Mutation Yes [3]
PDB Sequence
TVAYIAIGSN
10
LASPLEQVNA
20
ALKALGDIPE
30
SHILTVSSFY
40
RTPPPDYLNA
56

AVALETSLAP
66
EELLNHTQRI
76
ELQQGRGGPR
92
TLDLDIMLFG
102
NEVINTERLT
112

VPHYDMKNRG
122
FMLWPLFEIA
132
PELVFPDGEM
142
LRQILHTRAF
152
DKLNKW
Residue
Distance (Å)
GLY8
4.071
THR42
2.575
PRO43
2.604
PRO44
3.229
TYR53
3.234
Residue
Distance (Å)
ASN55
2.650
ASP95
2.803
ASP97
4.074
ARG121
4.128
PHE123
3.288
References  Top
REF 1 Dynamic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: crystallographic studies. Biochemistry. 2003 Feb 18;42(6):1573-80.
REF 2 Is the critical role of loop 3 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase in catalysis due to loop-3 residues arginine-84 and tryptophan-89? Site-directed mutagenesis, biochemical, and crystallographic studies. Biochemistry. 2005 Jun 21;44(24):8590-9.
REF 3 Essential roles of a dynamic loop in the catalysis of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase. Biochemistry. 2004 Feb 17;43(6):1469-77.

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